Regulation of respiration in brain mitochondria and synaptosomes: restrictions of ADP diffusion in situ, roles of tubulin, and mitochondrial creatine kinase
Abstract
The role of ubiquitous mitochondrial creatine kinase (uMtCK) reaction in regulation of mitochondrial respiration was studied in purified preparations of rat brain synaptosomes and mitochondria. In permeabilized synaptosomes, apparent Km for exogenous ADP, Km (ADP), in regulation of respiration in situ was rather high (110 +/- 11 microM) in comparison with isolated brain mitochondria (9 +/- 1 microM). This apparent Km for ADP observed in isolated mitochondria in vitro dramatically increased to 169 +/- 52 microM after their incubation with 1 muM of dimeric tubulin showing that in rat brain, particularly in synaptosomes, mitochondrial outer membrane permeability for ADP, and ATP may be restricted by tubulin binding to voltage dependent anion channel (VDAC). On the other hand, in synaptosomes apparent Km (ADP) decreased to 25 +/- 1 microM in the presence of 20 mM creatine. To fully understand this effect of creatine on kinetics of respiration regulation, complete kinetic analysis of uMtCK reaction in isolated brain mitochondria was carried out. This showed that oxidative phosphorylation specifically altered only the dissociation constants for MgATP, by decreasing that from ternary complex MtCK.Cr.MgATP (K (a)) from 0.13 +/- 0.02 to 0.018 +/- 0.007 mM and that from binary complex MtCK.MgATP (K (ia)) from 1.1 +/- 0.29 mM to 0.17 +/- 0.07 mM. Apparent decrease of dissociation constants for MgATP reflects effective cycling of ATP and ADP between uMtCK and adenine nucleotide translocase (ANT). These results emphasize important role and various pathophysiological implications of the phosphocreatine-creatine kinase system in energy transfer in brain cells, including synaptosomes.
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The beneficial effects of creatine supplementation on memory performance may be related to creatine's ability to influence brain bioenergetics.
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From Effects of creatine supplementation on memory in healthy individuals: a systematic review and meta-analysis of randomized controlled trials (2023) · cites this paper as [12]
In vitro, creatine elevates phosphocreatine and ATP levels and increases oxidative phosphorylation in synaptosomes and isolated brain mitochondria.
“In vitro, creatine elevates phosphocreatine and ATP levels11 and increases oxidative phosphorylation in synaptosomes and isolated brain mitochondria.12”
From Effects of creatine supplementation on memory in healthy individuals: a systematic review and meta-analysis of randomized controlled trials (2023) · cites this paper as [12]
Cites
Measurement of protein using bicinchoninic acid
Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., & Klenk, D. C. (1985) · Analytical Biochemistry · doi:10.1016/0003-2697(85)90442-7 · Cited by 18,482 · see citing works
Creatine and Creatinine Metabolism
Wyss, M., & Kaddurah-Daouk, R. (2000) · Physiological Reviews · doi:10.1152/physrev.2000.80.3.1107 · Cited by 2,950 · see citing works
Cleland, W. W. (1963) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(63)91800-6 · Cited by 2,092 · see citing works
Fundamentals of Enzyme Kinetics
Cornish-Bowden, A. J. (1979) · Elsevier eBooks · doi:10.1016/c2013-0-04130-8 · Cited by 2,079 · see citing works
The kinetics of enzyme-catalyzed reactions with two or more substrates or products
Cleland, W. W. (1963) · Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects · doi:10.1016/0926-6569(63)90211-6 · Cited by 1,911 · see citing works
Cleland, W. W. (1963) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(63)91815-8 · Cited by 867 · see citing works
The kinetics of enzyme-catalyzed reactions with two or more substrates or products
Cleland, W. W. (1963) · Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects · doi:10.1016/0926-6569(63)90227-x · Cited by 851 · see citing works
The kinetics of enzyme-catalyzed reactions with two or more substrates or products
Cleland, W. W. (1963) · Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects · doi:10.1016/0926-6569(63)90226-8 · Cited by 790 · see citing works
CNS energy metabolism as related to function
Ames, A. (2000) · Brain Research Reviews · doi:10.1016/s0165-0173(00)00038-2 · Cited by 663 · see citing works
Encyclopedia of biological chemistry
(2013) · Choice Reviews Online · doi:10.5860/choice.51-0034 · Cited by 558 · see citing works
The Conduction of the Nervous Impulse
Landau, W. M. (1965) · Neurology · doi:10.1212/wnl.15.6.595 · Cited by 540 · see citing works
The Machinery of Mitochondrial Inheritance and Behavior
Yaffe, M. P. (1999) · Science · doi:10.1126/science.283.5407.1493 · Cited by 496 · see citing works
Phosphotransfer networks and cellular energetics
Dzeja, P. P., & Terzic, A. (2003) · Journal of Experimental Biology · doi:10.1242/jeb.00426 · Cited by 472 · see citing works
Creatine Kinase of Rat Heart Mitochondria
Jacobus, W. E., & Lehninger, A. L. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43737-x · Cited by 469 · see citing works
BOOTH, R. F. G., & Clark, J. B. (1978) · Biochemical Journal · doi:10.1042/bj1760365 · Cited by 469 · see citing works
Mitochondrial creatine kinase: a key enzyme of aerobic energy metabolism
Wyss, M., Smeitink, J. A. M., Wevers, R. A., & Wallimann, T. (1992) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(92)90096-k · Cited by 443 · see citing works
Fundamentals of enzyme kinetics
Selwyn, M. (1996) · Biochemical Education · doi:10.1016/s0307-4412(96)80014-8 · Cited by 434 · see citing works
SCOTT, I. D., & Nicholls, D. G. (1980) · Biochemical Journal · doi:10.1042/bj1860021 · Cited by 394 · see citing works
Mitochondrial Trafficking to Synapses in Cultured Primary Cortical Neurons
Chang, D. T. W., Honick, A. S., & Reynolds, I. J. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1012-06.2006 · Cited by 391 · see citing works
Creatine kinase in non-muscle tissues and cells
Wallimann, T., & Hemmer, W. (1994) · Molecular and Cellular Biochemistry · doi:10.1007/bf01267955 · Cited by 375 · see citing works
Functions and effects of creatine in the central nervous system
Andres, R. H., Ducray, A., Schlattner, U., Wallimann, T., & Widmer, H. R. (2008) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2008.02.035 · Cited by 372 · see citing works
Self-citationPermeabilized cell and skinned fiber techniques in studies of mitochondrial function in vivo
Saks, V. A., Veksler, V., Kuznetsov, A. V., Kay, L., Sikk, P., Tiivel, T., Tranqui, L., Olivares, J., Winkler, K., Wiedemann, F. R., et al. (1998) · Springer eBooks · doi:10.1007/978-1-4615-5653-4_7 · Cited by 361 · see citing works
Self-citationRostovtseva, T. K., & Colombini, M. (1997) · Biophysical Journal · doi:10.1016/s0006-3495(97)78841-6 · Cited by 357 · see citing works
Self-citationHandbook of Neurochemistry and Molecular Neurobiology
Lajtha, Á., Galoyan, A. A., & Besedovsky, H. O. (2007) · Springer eBooks · doi:10.1007/978-0-387-30398-7 · Cited by 350 · see citing works
On cytochrome c oxidase I. The extinction coefficients of cytochrome a and cytochrome a3
GELDER, B. F. V. (1966) · Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation · doi:10.1016/s0926-6593(66)80142-x · Cited by 327 · see citing works
Caldwell, P. C., Hodgkin, A. L., Keynes, R. D., & Shaw, T. I. (1960) · The Journal of Physiology · doi:10.1113/jphysiol.1960.sp006509 · Cited by 321 · see citing works
Permeabilized cell and skinned fiber techniques in studies of mitochondrial function in vitro
Veksler, V., Kuznetsov, A. V., Kay, L., Sikk, P., Tiivel, T., Tranqui, L., Olivares, J., Winkler, K., Wiedemann, F. R., & Kunz, W. S. (1998) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006834912257 · Cited by 308 · see citing works
Self-citationAzzi, A. (1980) · Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics · doi:10.1016/0304-4173(80)90002-6 · Cited by 303 · see citing works
Energy metabolism in mammalian brain during development
Erecińska, M., Cherian, S., & Silver, I. A. (2004) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2004.06.003 · Cited by 299 · see citing works
Carreá, M., André, N., Carles, G., Borghi, H., Brichese, L., Briand, C. M., & Braguer, D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203834200 · Cited by 273 · see citing works
(2000) · Springer eBooks · doi:10.1007/978-3-662-04162-8 · Cited by 260 · see citing works
Cardiac system bioenergetics: metabolic basis of the Frank‐Starling law
Saks, V. A., Dzeja, P. P., Schlattner, U., Vendelin, M., Terzic, A., & Wallimann, T. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2005.101444 · Cited by 251 · see citing works
Self-citationSaks, V. A., Chernousova, G. B., GUKOVSKY, D. E., SMIRNOV, V. N., & Чазов, Е. И. (1975) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1975.tb02299.x · Cited by 244 · see citing works
Self-citationDesmin Cytoskeleton A Potential Regulator of Muscle Mitochondrial Behavior and Function
Capetanaki, Y. (2002) · Trends in Cardiovascular Medicine · doi:10.1016/s1050-1738(02)00184-6 · Cited by 224 · see citing works
Relating Structure to Mechanism in Creatine Kinase
McLeish, M. J., & Kenyon, G. L. (2005) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230590918577 · Cited by 214 · see citing works
Wyss, M., & Schulze, A. (2002) · Neuroscience · doi:10.1016/s0306-4522(02)00088-x · Cited by 210 · see citing works
Mitochondrial Creatine Kinase Activity Prevents Reactive Oxygen Species Generation
Meyer, L. E., Machado, L. B., Santiago, A. P. S. A., da‐Silva, W. S., Felice, F. G. D., Holub, O., de Oliveira, M. F., & Galina, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604123200 · Cited by 210 · see citing works
Gnaiger, E., Kuznetsov, A. V., Schneeberger, S., Seiler, R., Brandacher, G., Steurer, W., & Margreiter, R. (2000) · Springer eBooks · doi:10.1007/978-3-662-04162-8_45 · Cited by 208 · see citing works
Self-citationEGTA purity and the buffering of calcium ions in physiological solutions
Miller, D. J., & Smith, G. L. (1984) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1984.246.1.c160 · Cited by 208 · see citing works
Chen, C., Ko, Y. H., Delannoy, M. R., Ludtke, S. J., Chiu, W., & Pedersen, P. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401353200 · Cited by 206 · see citing works
Mitochondrial regular arrangement in muscle cells: a “crystal-like” pattern
Vendelin, M., Béraud, N., Guerrero, K., Andrienko, T., Kuznetsov, A. V., Olivares, J., Kay, L., & Saks, V. A. (2005) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00281.2004 · Cited by 193 · see citing works
Self-citationSaks, V. A., Kuznetsov, A. V., Kupriyanov, V. V., Miceli, M. V., & Jacobus, W. E. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39672-2 · Cited by 189 · see citing works
Self-citationIntracellular energetic units in red muscle cells
Saks, V. A., Käämbre, T., Sikk, P., Eimre, M., Orlova, E., Paju, K., Piirsoo, A., Appaix, F., Kay, L., Regitz‐Zagrosek, V., et al. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3560643 · Cited by 187 · see citing works
Self-citationKuznetsov, A. V., Schneeberger, S., Seiler, R., Brandacher, G., Mark, W., Steurer, W., Saks, V. A., Usson, Y., Margreiter, R., & Gnaiger, E. (2004) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00701.2003 · Cited by 168 · see citing works
Self-citationSaks, V. A., Kuznetsov, A. V., Khuchua, Z. A., Vasilyeva, E. V., BELIKOVA, J., Kesvatera, T., & Tiivel, T. (1995) · Journal of Molecular and Cellular Cardiology · doi:10.1016/s0022-2828(08)80056-9 · Cited by 164 · see citing works
Self-citationJost, C. R., der Zee, C. E. E. M. V., Zandt, R. I. ‘., Oerlemans, F. T. J. J., Verheij, M. M. M., Streijger, F., Fransen, J. A. M., Heerschap, A., Cools, A. R., & Wieringa, B. (2002) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2002.02001.x · Cited by 161 · see citing works
Possible Role of Cytoskeleton in Intracellular Arrangement and Regulation of Mitochondria
Appaix, F., Kuznetsov, A. V., Usson, Y., et al. (2003) · Experimental Physiology · doi:10.1113/eph8802511 · Cited by 152 · see citing works
Self-citationCardiolipin is the membrane receptor for mitochondrial creatine phosphokinase.
Müller, M., Moser, R., Cheneval, D., & Carafoli, E. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83700-6 · Cited by 142 · see citing works
Intracellular energetic units in red muscle cells
Saks, V. A., Käämbre, T., Sikk, P., et al. (2001) · Biochemical Journal · doi:10.1042/bj3560643 · Cited by 134 · see citing works
Self-citationLeterrier, J. F., Rusakov, D. A., Nelson, B. D., et al. (1994) · Microscopy Research and Technique · doi:10.1002/jemt.1070270305 · Cited by 131 · see citing works
Jacobus, W. E., & Saks, V. A. (1982) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(82)90146-1 · Cited by 129 · see citing works
Self-citationStudies on adenosine triphosphate transphosphorylases
Keutel, H. J., Okabe, K., Jacobs, H. K., et al. (1972) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(72)90085-9 · Cited by 126 · see citing works
Creatine Kinase: Structure‐Activity Relationships
Kenyon, G. L., & Reed, G. H. (1983) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122990.ch6 · Cited by 125 · see citing works
Scholte, H. R., Weijers, P. J., & Wit-Peeters, E. M. (1973) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(73)90479-3 · Cited by 118 · see citing works
Structural and behavioural consequences of double deficiency for creatine kinases BCK and UbCKmit
Streijger, F., Oerlemans, F. T. J. J., Ellenbroek, B. A., Jost, C. R., Wieringa, B., & VANDERZEE, C. (2004) · Behavioural Brain Research · doi:10.1016/j.bbr.2004.07.002 · Cited by 104 · see citing works
SCOTT, I. D., Åkerman, K. E. O., & Nicholls, D. G. (1980) · Biochemical Journal · doi:10.1042/bj1920873 · Cited by 102 · see citing works
Song, J., Midson, C. N., Blachly‐Dyson, E., Forte, M. A., & Colombini, M. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)78000-2 · Cited by 99 · see citing works
Heterogeneity of ADP Diffusion and Regulation of Respiration in Cardiac Cells
Saks, V. A., Kuznetsov, A., Andrienko, T., Usson, Y., Appaix, F., Guerrero, K., Käämbre, T., Sikk, P., Lemba, M., & Vendelin, M. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)70065-4 · Cited by 91 · see citing works
Self-citationThe role of cytochrome c diffusion in mitochondrial electron transport.
Gupte, S. S., & Hackenbrock, C. R. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60707-0 · Cited by 88 · see citing works
Intracellular diffusion of adenosine phosphates is locally restricted in cardiac muscle
Vendelin, M., Eimre, M., Seppet, E., Peet, N., Andrienko, T., Lemba, M., Engelbrecht, J., Seppet, E. K., & Saks, V. A. (2003) · Molecular and Cellular Biochemistry · doi:10.1023/b:mcbi.0000009871.04141.64 · Cited by 88 · see citing works
Self-citationWallimann, T., Tokarska-Schlattner, M., Neumann, D., Epand, R. M., Epand, R. F., Andres, R. H., Widmer, H. R., Hornemann, T., Saks, V. A., Agarkova, I., et al. (2007) · Wiley eBooks · doi:10.1002/9783527621095.ch7 · Cited by 81 · see citing works
Self-citationAnalysis of Functional Coupling: Mitochondrial Creatine Kinase and Adenine Nucleotide Translocase
Vendelin, M., Lemba, M., & Saks, V. A. (2004) · Biophysical Journal · doi:10.1529/biophysj.103.036210 · Cited by 77 · see citing works
Self-citationLim, L., Hall, C., LEUNG, T. K. C., Mahadevan, L. C., & Whatley, S. A. (1983) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1983.tb09069.x · Cited by 74 · see citing works
Bioenergetics and Transmitter Release in the Isolated Nerve Terminal
Nicholls, D. G. (2003) · Neurochemical Research · doi:10.1023/a:1025653805029 · Cited by 71 · see citing works
C-terminal Lysines Determine Phospholipid Interaction of Sarcomeric Mitochondrial Creatine Kinase
Schlattner, U., Gehring, F., Vernoux, N., Tokarska-Schlattner, M., Neumann, D., Marcillat, O., Vial, C., & Wallimann, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314158200 · Cited by 71 · see citing works
Self-citationFriedman, D. L., & Roberts, R. (1994) · The Journal of Comparative Neurology · doi:10.1002/cne.903430311 · Cited by 68 · see citing works
Zandt, R. I. ‘., Renema, W. K. J., Streijger, F., Jost, C. R., Klomp, D. W. J., Oerlemans, F. T. J. J., van der Zee, C. E. E. M., Wieringa, B., & Heerschap, A. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02599.x · Cited by 60 · see citing works
Lindén, M., Nelson, B. D., & Leterrier, J. F. (1989) · Biochemical Journal · doi:10.1042/bj2610167 · Cited by 59 · see citing works
Molecular System Bioenergetics
(2007) · Wiley eBooks · doi:10.1002/9783527621095 · Cited by 58 · see citing works
Cation selective promotion of tubulin polymerization by alkali metal chlorides
Wolff, J., Sackett, D., & Knipling, L. G. (1996) · Protein Science · doi:10.1002/pro.5560051008 · Cited by 57 · see citing works
Self-citationInteraction of tubulin with rat liver mitochondria.
Bernier‐Valentin, F., & Rousset, B. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34541-1 · Cited by 56 · see citing works
Studies on Adenosine Triphosphate Transphosphorylases
Jacobs, H. K., & Kuby, S. A. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62996-5 · Cited by 55 · see citing works
Kinetic Mechanism of the p38-α MAP Kinase: Phosphoryl Transfer to Synthetic Peptides
Chen, G., Porter, M. D., Bristol, J. R., et al. (2000) · Biochemistry · doi:10.1021/bi9919495 · Cited by 54 · see citing works
Metabolic and energetic properties of isolated nerve ending particles (synaptosomes)
Erecińska, M., NELSON, D. S., & Silver, I. A. (1996) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(96)00103-x · Cited by 51 · see citing works
Kuznetsov, A. V., Khuchua, Z. A., Vassil'eva, E. V., et al. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90578-x · Cited by 50 · see citing works
Self-citationIsolation of microtubule protein from mammalian brain frozen for extended periods of time
Sackett, D. L., Knipling, L., & Wolff, J. (1991) · Protein Expression and Purification · doi:10.1016/1046-5928(91)90099-5 · Cited by 37 · see citing works
Self-citationCreatine kinase isoenzyme associated with synaptosomal membrane and synaptic vesicles
Friedhoff, A. J., & Lerner, M. H. (1977) · Life Sciences · doi:10.1016/0024-3205(77)90039-x · Cited by 36 · see citing works
The rate of formation and turnover of phosphorus compounds in squid giant axons
Caldwell, P. C., Hodgkin, A. L., Keynes, R. D., et al. (1964) · The Journal of Physiology · doi:10.1113/jphysiol.1964.sp007366 · Cited by 36 · see citing works
Brain energetics, integration of molecular and cellular processes
Lajtha, Á., Gibson, G. E., & Dienel, G. A. (2007) · Springer eBooks · Cited by 33 · see citing works
Metabolite Channeling: Creatine Kinase Microcompartments
Schlattner, U., Tokarska-Schlattner, M., & Wallimann, T. (2013) · Encyclopedia of Biological Chemistry · doi:10.1016/b978-0-12-378630-2.00283-8 · Cited by 30 · see citing works
Self-citationTesting a Novel Strategy Against Parkinson's Disease
Couzin, J. (2007) · Science · doi:10.1126/science.315.5820.1778 · Cited by 30 · see citing works
Bax and heart mitochondria: uncoupling and inhibition of respiration without permeability transition
Appaix, F., Guerrero, K., Rampal, D., et al. (2002) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(02)00358-4 · Cited by 25 · see citing works
Comparison of kinetic constants of creatine kinase isoforms
Matsushima, K., Uda, K., Ishida, K., Kokufuta, C., Iwasaki, N., & Suzuki, T. (2006) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2005.12.023 · Cited by 22 · see citing works
Kinetic mechanism for p38 MAP kinase α
Szafranska, A. E., & Dalby, K. N. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.04827.x · Cited by 21 · see citing works
Aliev, M., van Dorsten, F. A., Nederhoff, M. G. J., van Echteld, C. J. A., Veksler, V., Nicolay, K., & Saks, V. A. (1998) · Springer eBooks · doi:10.1007/978-1-4615-5653-4_16 · Cited by 20 · see citing works
Self-citationMetabolite Channeling: Creatine Kinase Microcompartments
Schlattner, U., & Wallimann, T. (2004) · Encyclopedia of Biological Chemistry · doi:10.1016/b0-12-443710-9/00642-6 · Cited by 16 · see citing works
Self-citationRossi, A., Kay, L., & Saks, V. A. (1998) · PubMed · Cited by 13 · see citing works
Self-citation8.1 Mechanisms and Modeling of Energy Transfer Between Intracellular Compartments
Saks, V. A., Vendelin, M., Aliev, M., Kekelidze, T., & Engelbrecht, J. (2007) · Springer eBooks · doi:10.1007/978-0-387-30411-3_30 · Cited by 11 · see citing works
Self-citationRossi, A., Kay, L., & Saks, V. (1998) · Molecular and Cellular Biochemistry · doi:10.1023/a:1006874825403 · Cited by 11 · see citing works
Self-citationDzeja, P. P., & Terzic, A. (2007) · Springer eBooks · doi:10.1007/978-0-387-30411-3_24 · Cited by 10 · see citing works
Structural Organization and Dynamics of Mitochondria in the Cells in Vivo
Kuznetsov, A. V. (2007) · Wiley eBooks · doi:10.1002/9783527621095.ch5 · Cited by 3 · see citing works
Self-citationIntroduction: From the Discovery of Biological Oxidation to Molecular System Bioenergetics
Saks, V. (2007) · doi:10.1002/9783527621095.ch · Cited by 2 · see citing works
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Self-citationProkopidis, K., Giannos, P., Triantafyllidis, K. K., Kechagias, K. S., Forbes, S. C., & Candow, D. G. (2023) · Nutrition Reviews · doi:10.1093/nutrit/nuac064 · Cited by 71 · see citing works
Snow, W. M., Cadonic, C., Cortes-Perez, C., Roy Chowdhury, S. K., Djordjevic, J., Thomson, E., Bernstein, M. J., Suh, M., Fernyhough, P., & Albensi, B. C. (2018) · Learning & Memory · doi:10.1101/lm.046284.117 · Cited by 31 · see citing works
- Authors
- Monge, C., Beraud, N., Kuznetsov, A. V., Rostovtseva, T., Sackett, D., Schlattner, U., Vendelin, M., & Saks, V. A.
- Affiliations
- Université Joseph Fourier (FR)
- National Institutes of Health (US)
- Tallinn University of Technology (EE)
- Corresponding author
- Saks, Valdur A.
- ORCID
- Venue
- Molecular and Cellular Biochemistry
- Published
- 2008-07-16
- Volume
- 318
- Issue
- 1-2
- Pages
- 147-165
- ISSN
- 0300-8177 (ISSN-L)
- 1573-4919
- OpenAlex
- W2015492989
- Cited by
- 85
- References
- 92
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 3 · 2022: 8 · 2021: 3 · 2020: 5 · 2019: 2 · 2018: 4 · 2017: 3 · 2016: 4 · 2015: 4 · 2014: 6 · 2013: 8 · 2012: 6
- FWCI
- 3.55
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Molecular and Cellular Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Institut National de la Santé et de la Recherche Médicale
- Eesti Teadusfondi
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- mitochondrial creatine kinase, brain mitochondria, synaptosomes, tubulin, voltage-dependent anion channel, mitochondrial outer membrane permeability, creatine, adenine nucleotide translocase, oxidative phosphorylation, energy transfer
- MeSH terms
- Mitochondrial ADP, ATP Translocases, Adenosine Diphosphate, Animals, Brain, Creatine, Diffusion, Electron Transport, Energy Metabolism, Isoenzymes, Kinetics, Male, Mitochondria, Mitochondria, Heart, Permeability, Synaptosomes, Tissue Extracts, Tubulin, Rats, Wistar, Microscopy, Confocal, Cell Respiration, Rats, Creatine Kinase, Mitochondrial Form
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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